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Bioinspired production of magnetic laccase-biotitania particles for the removal of endocrine disrupting chemicals

Bibliographic reference Ardao Palacios , Inés ; Magnin, Delphine ; Agathos, Spiros N.. Bioinspired production of magnetic laccase-biotitania particles for the removal of endocrine disrupting chemicals. In: Biotechnology and Bioengineering, Vol. 112, no.10, p. 1986-1996 (2015)
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  1. Ansari Shakeel Ahmed, Husain Qayyum, Potential applications of enzymes immobilized on/in nano materials: A review, 10.1016/j.biotechadv.2011.09.005
  2. Arboleda Carolina, Cabana H., De Pril E., Jones J. Peter, Jiménez G. A., Mejía A. I., Agathos S. N., Penninckx M. J., Elimination of Bisphenol A and Triclosan Using the Enzymatic System of Autochthonous Colombian Forest Fungi, 10.5402/2013/968241
  3. Ardao Inés, Alvaro Gregorio, Benaiges M. Dolors, Reversible immobilization of rhamnulose-1-phosphate aldolase for biocatalysis: Enzyme loading optimization and aldol addition kinetic modeling, 10.1016/j.bej.2011.06.007
  4. Ardao Inés, Comenge Joan, Benaiges M. Dolors, Álvaro Gregorio, Puntes Víctor F., Rational Nanoconjugation Improves Biocatalytic Performance of Enzymes: Aldol Addition Catalyzed by Immobilized Rhamnulose-1-Phosphate Aldolase, 10.1021/la3003993
  5. Ardao Inés, Hwang Ee Taek, Zeng An-Ping, In Vitro Multienzymatic Reaction Systems for Biosynthesis, Fundamentals and Application of New Bioproduction Systems (2013) ISBN:9783642415203 p.153-184, 10.1007/10_2013_232
  6. Ba Sidy, Arsenault Alexandre, Hassani Thanina, Jones J. Peter, Cabana Hubert, Laccase immobilization and insolubilization: from fundamentals to applications for the elimination of emerging contaminants in wastewater treatment, 10.3109/07388551.2012.725390
  7. Barros Raúl J., Wehtje Ernst, Adlercreutz Patrick, Mass transfer studies on immobilized α-chymotrypsin biocatalysts prepared by deposition for use in organic medium, 10.1002/(sici)1097-0290(19980805)59:3<364::aid-bit13>;2-e
  8. Bastin G. F., Dijkstra J. M., Heijligers H. J. M., PROZA96: an improved matrix correction program for electron probe microanalysis, based on a double Gaussian ϕ(ρz) approach, 10.1002/(sici)1097-4539(199801/02)27:1<3::aid-xrs227>;2-l
  9. Berrio Jimmy, Plou Francisco J., Ballesteros Antonio, Martínez Ángel T., Martínez María Jesús, Immobilization ofpycnoporus coccineuslaccase on Eupergit C: Stabilization and treatment of olive oil mill wastewaters, 10.1080/10242420701379122
  10. Betancor Lorena, Luckarift Heather R., Bioinspired enzyme encapsulation for biocatalysis, 10.1016/j.tibtech.2008.06.009
  11. Bonsack James P, Ion-exchange and surface properties of titania gels from Ti(IV) sulfate solutions, 10.1016/0021-9797(73)90319-6
  12. Boon, Microchimica Acta, 147, 125 (2004)
  13. Brena Beatriz M., Batista-Viera Francisco, Immobilization of Enzymes, Immobilization of Enzymes and Cells (2006) ISBN:9781588292902 p.15-30, 10.1007/978-1-59745-053-9_2
  14. Brutchey Richard L., Morse Daniel E., Silicatein and the Translation of its Molecular Mechanism of Biosilicification into Low Temperature Nanomaterial Synthesis, 10.1021/cr078256b
  15. Cabana H., Jones J. P., Agathos S. N., Elimination of Endocrine Disrupting Chemicals using White Rot Fungi and their Lignin Modifying Enzymes: A Review, 10.1002/elsc.200700017
  16. Cabana Hubert, Jones J. Peter, Agathos Spiros N., Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals, 10.1002/bit.22198
  17. Caliman, CLEAN, 37, 277 (2009)
  18. Chen Xiaobo, Mao Samuel S., Titanium Dioxide Nanomaterials:  Synthesis, Properties, Modifications, and Applications, 10.1021/cr0500535
  19. Cumana Sucre, Ardao Inés, Zeng An-Ping, Smirnova Irina, Glucose-6-phosphate dehydrogenase encapsulated in silica-based hydrogels for operation in a microreactor, 10.1002/elsc.201300062
  20. Daughton Christian G., Non-regulated water contaminants: emerging research, 10.1016/j.eiar.2004.06.003
  21. Deblonde Tiphanie, Cossu-Leguille Carole, Hartemann Philippe, Emerging pollutants in wastewater: A review of the literature, 10.1016/j.ijheh.2011.08.002
  22. Demarche Philippe, Junghanns Charles, Mazy Nicolas, Agathos Spiros N., Design-of-experiment strategy for the formulation of laccase biocatalysts and their application to degrade bisphenol A, 10.1016/j.nbt.2012.05.023
  23. Demarche Philippe, Junghanns Charles, Nair Rakesh R., Agathos Spiros N., Harnessing the power of enzymes for environmental stewardship, 10.1016/j.biotechadv.2011.05.013
  24. Durán Nelson, Esposito Elisa, Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: a review, 10.1016/s0926-3373(00)00168-5
  25. Durán Nelson, Rosa Maria A, D’Annibale Alessandro, Gianfreda Liliana, Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review, 10.1016/s0141-0229(02)00214-4
  26. Fernández-Fernández María, Sanromán M. Ángeles, Moldes Diego, Recent developments and applications of immobilized laccase, 10.1016/j.biotechadv.2012.02.013
  27. Fogler, Elements of chemical reaction engineering (2006)
  28. García-González C.A., Sousa A.R. Sampaio da, Argemí A., Periago A. López, Saurina J., Duarte C.M.M., Domingo C., Production of hybrid lipid-based particles loaded with inorganic nanoparticles and active compounds for prolonged topical release, 10.1016/j.ijpharm.2009.08.033
  29. García-González Carlos A., Carenza Elisa, Zeng Muling, Smirnova Irina, Roig Anna, Design of biocompatible magnetic pectin aerogel monoliths and microspheres, 10.1039/c2ra21500d
  30. Gavrilescu Maria, Demnerová Kateřina, Aamand Jens, Agathos Spiros, Fava Fabio, Emerging pollutants in the environment: present and future challenges in biomonitoring, ecological risks and bioremediation, 10.1016/j.nbt.2014.01.001
  31. Gavrilescu, Environ Eng Manage J, 8, 1517 (2009)
  32. Homaei Ahmad Abolpour, Sariri Reyhaneh, Vianello Fabio, Stevanato Roberto, Enzyme immobilization: an update, 10.1007/s12154-013-0102-9
  33. Hwang Ee Taek, Gu Man Bock, Enzyme stabilization by nano/microsized hybrid materials : Enzyme stabilization by nano/microsized hybrid materials, 10.1002/elsc.201100225
  34. Iversen S.B., Bhatia V.K., Dam-Johansen K., Jonsson G., Characterization of microporous membranes for use in membrane contactors, 10.1016/s0376-7388(97)00026-4
  35. Jiang Yanjun, Sun Qianyun, Jiang Zhongyi, Zhang Lei, Li Jian, Li Lin, Sun Xiaohui, The improved stability of enzyme encapsulated in biomimetic titania particles, 10.1016/j.msec.2008.07.006
  36. Kim Jungbae, Grate Jay W., Wang Ping, Nanostructures for enzyme stabilization, 10.1016/j.ces.2005.05.067
  37. Kröger Nils, Dickerson Matthew B., Ahmad Gul, Cai Ye, Haluska Michael S., Sandhage Kenneth H., Poulsen Nicole, Sheppard Vonda C., Bioenabled Synthesis of Rutile (TiO2) at Ambient Temperature and Neutral pH, 10.1002/anie.200601871
  38. Kurniawati Selvia, Nicell James A., Characterization of Trametes versicolor laccase for the transformation of aqueous phenol, 10.1016/j.biortech.2008.01.084
  39. Kyotani Tomohiro, Koshimizu Satoshi, Identification of Individual Si-Rich Particles Derived from Kosa Aerosol by the Alkali Elemental Composition, 10.1246/bcsj.74.723
  40. Laurent Sophie, Forge Delphine, Port Marc, Roch Alain, Robic Caroline, Vander Elst Luce, Muller Robert N., Magnetic Iron Oxide Nanoparticles: Synthesis, Stabilization, Vectorization, Physicochemical Characterizations, and Biological Applications, 10.1021/cr068445e
  41. Lloret L., Hollmann F., Eibes G., Feijoo G., Moreira M. T., Lema J. M., Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor, 10.1007/s10532-011-9516-7
  42. Margot Jonas, Bennati-Granier Chloé, Maillard Julien, Blánquez Paqui, Barry David A, Holliger Christof, Bacterial versus fungal laccase: potential for micropollutant degradation, 10.1186/2191-0855-3-63
  43. Mezedur Minas M., Kaviany Massoud, Moore Wayne, Effect of pore structure, randomness and size on effective mass diffusivity, 10.1002/aic.690480104
  44. Müller Werner E. G., Link Thorben, Li Qiang, Schröder Heinz C., Batel Renato, Blažina Maria, Grebenjuk Vladislav A., Wang Xiaohong, A novel TiO2-assisted magnetic nanoparticle separator for treatment and inactivation of bacterial contaminants in aquatic systems, 10.1039/c4ra09055a
  45. Nair Rakesh R., Demarche Philippe, Agathos Spiros N., Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater, 10.1016/j.nbt.2012.12.004
  46. Osán J., de Hoog J., Van Espen P., Szalóki I., Ro C.-U., Van Grieken R., Evaluation of energy-dispersive x-ray spectra of low-Zelements from electron-probe microanalysis of individual particles : EDXRF spectra of low-Zelements, 10.1002/xrs.523
  47. Paloheimo M Valtakari L Puranen T Kruus K Kallio J Mäntylä A Fagerström R Ojapalo P Vehmaanperä J 2011 AB Enzymes OY, assignee. 2011 Apr. 19. Novel laccase enzyme and use thereof
  48. Preda, Environ Eng Manage J, 11, 1697 (2012)
  49. Richardson Susan D., Ternes Thomas A., Water Analysis: Emerging Contaminants and Current Issues, 10.1021/ac200915r
  50. Richardson Susan D., Water Analysis: Emerging Contaminants and Current Issues, 10.1021/ac9008012
  51. Rogers James A., Metz Luanne, Yong V. Wee, Review: Endocrine disrupting chemicals and immune responses: A focus on bisphenol-A and its potential mechanisms, 10.1016/j.molimm.2012.09.013
  52. Roig Benoit, Mnif Wissem, Hadj Hassine Aziza Ibn, Zidi Ines, Bayle Sandrine, Bartegi Aghleb, Thomas Olivier, Endocrine Disrupting Chemicals and Human Health Risk Assessment: A Critical Review, 10.1080/10643389.2012.672076
  53. Sano Kazuhiro, Doi Masao, Theory of Agglomeration of Ferromagnetic Particles in Magnetic Fluids, 10.1143/jpsj.52.2810
  54. Sheldon Roger A., Enzyme Immobilization: The Quest for Optimum Performance, 10.1002/adsc.200700082
  55. Shi, J Environ Anal Toxicol, S2, 003 (2012)
  56. Shukoor Mohammed Ibrahim, Natalio Filipe, Therese Helen Annal, Tahir Muhammad Nawaz, Ksenofontov Vadim, Panthöfer Martin, Eberhardt Marc, Theato Patrick, Schröder Heinz Christoph, Müller Werner E. G., Tremel Wolfgang, Fabrication of a Silica Coating on Magnetic γ-Fe2O3Nanoparticles by an Immobilized Enzyme, 10.1021/cm7029954
  57. Sumerel Jan L., Yang Wenjun, Kisailus David, Weaver James C., Choi Joon Hwan, Morse Daniel E., Biocatalytically Templated Synthesis of Titanium Dioxide, 10.1021/cm030254u
  58. Sun Qianyun, Jiang Yanjun, Jiang Zhongyi, Zhang Lei, Sun Xiaohui, Li Jian, Green and Efficient Conversion of CO2to Methanol by Biomimetic Coimmobilization of Three Dehydrogenases in Protamine-Templated Titania, 10.1021/ie801931j
  59. Tampieri Anna, Iafisco Michele, Sandri Monica, Panseri Silvia, Cunha Carla, Sprio Simone, Savini Elisa, Uhlarz Marc, Herrmannsdörfer Thomas, Magnetic Bioinspired Hybrid Nanostructured Collagen–Hydroxyapatite Scaffolds Supporting Cell Proliferation and Tuning Regenerative Process, 10.1021/am5050967
  60. Templeton M. R., Graham N., Voulvoulis N., Emerging chemical contaminants in water and wastewater, 10.1098/rsta.2009.0144
  61. Tong Zhenwei, Jiang Yanjun, Yang Dong, Shi Jiafu, Zhang Shaohua, Liu Chuang, Jiang Zhongyi, Biomimetic and bioinspired synthesis of titania and titania-based materials, 10.1039/c3ra47336h
  62. Torres Eduardo, Bustos-Jaimes Ismael, Le Borgne Sylvie, Potential use of oxidative enzymes for the detoxification of organic pollutants, 10.1016/s0926-3373(03)00228-5
  63. van Espen, Handbook of X-ray spectrometry: Methods and techniques, 181 (1993)
  64. Wang Xiaoliang, Zhou Linzhu, Ma Yongjie, Li Xu, Gu Hongchen, Control of aggregate size of polyethyleneimine-coated magnetic nanoparticles for magnetofection, 10.1007/s12274-009-9035-6
  65. Wilke C. R., Chang Pin, Correlation of diffusion coefficients in dilute solutions, 10.1002/aic.690010222
  66. Won Yu-Ho, Jang Ho Seong, Kim Seung Min, Stach Eric, Ganesana Mallikarjunarao, Andreescu Silvana, Stanciu Lia A., Biomagnetic Glasses: Preparation, Characterization, and Biosensor Applications, 10.1021/la903422q
  67. Zhang Dong-Hao, Yuwen Li-Xia, Peng Li-Juan, Parameters Affecting the Performance of Immobilized Enzyme, 10.1155/2013/946248